Mca-SEVNLDAEFK(Dnp)-NH2 integrates a fluorescent donor and quencher pair within a protease-sensitive peptide. Residue arrangement supports kinetic studies of cleavage events. Researchers track fluorescence restoration to measure catalytic rates. Uses include enzyme profiling, mechanistic evaluation, and substrate design.
CAT No: R2541
CAS No:1802078-32-5
Synonyms/Alias:1802078-32-5;Mca-SEVNLDAEFK(Dnp)-NH2;Mca-(Asn670,Leu671)-Amyloid b/A4 Protein Precursor770 (667-675)-Lys(Dnp) amide Ammonium;Mca-(Asn670,Leu671)-Amyloid beta/A4 Protein Precursor770 (667-675)-Lys(Dnp) amide ammonium salt;Unk-Ser-Glu-Val-Asn-Leu-Asp-Ala-Glu-Phe-Lys(Dnp)-NH2;HY-P4920;FM110963;CS-0674983;
Mca-SEVNLDAEFK(Dnp)-NH2 is a synthetic peptide substrate widely recognized for its utility in biochemical research, particularly in the study of protease activity and enzyme kinetics. Featuring a 7-methoxycoumarin-4-acetyl (Mca) fluorophore at the N-terminus and a 2,4-dinitrophenyl (Dnp) quencher at the lysine residue, this FRET-based substrate is engineered to facilitate sensitive and real-time detection of proteolytic cleavage. The peptide sequence SEVNLDAEFK is designed to mimic specific cleavage sites, making it an invaluable tool for researchers investigating the specificity and efficiency of various proteases. Its robust fluorescence quenching and release mechanism upon enzymatic hydrolysis enable highly quantitative and reproducible measurements, supporting advanced studies in enzyme characterization, inhibitor screening, and biochemical assay development.
Protease Activity Assays: Mca-SEVNLDAEFK(Dnp)-NH2 is extensively employed in protease activity assays, where its FRET-based design allows for the continuous monitoring of enzymatic reactions. Upon cleavage by target proteases, the spatial separation of the Mca fluorophore from the Dnp quencher results in a measurable increase in fluorescence intensity, providing a direct and sensitive readout of proteolytic activity. This mechanism offers significant advantages in terms of assay speed, sensitivity, and the ability to conduct high-throughput screening for protease inhibitors or activators, facilitating drug discovery and basic research into protease function.
Enzyme Kinetics Studies: The substrate is a preferred choice for enzyme kinetics studies due to its precise and quantifiable response to protease-mediated cleavage. Researchers utilize this peptide to determine key kinetic parameters such as Km and Vmax, enabling the detailed characterization of enzyme-substrate interactions. By monitoring fluorescence changes in real-time, scientists can accurately assess the catalytic efficiency and substrate specificity of proteolytic enzymes, supporting both fundamental enzymology and the development of novel enzymatic assays.
High-Throughput Screening: In pharmaceutical and academic research environments, Mca-SEVNLDAEFK(Dnp)-NH2 serves as an essential reagent for high-throughput screening (HTS) of protease modulators. Its compatibility with automated fluorescence plate readers allows for rapid and parallel analysis of thousands of compounds, accelerating the identification of potential enzyme inhibitors or activators. The substrate's robust signal-to-noise ratio and reproducibility contribute to reliable data generation, making it a cornerstone in the workflow of drug discovery programs focused on proteolytic targets.
Substrate Specificity Profiling: Researchers leverage this peptide to profile the substrate specificity of various proteases, including those involved in physiological and pathological processes. By analyzing the cleavage efficiency and site preference, scientists can elucidate the molecular determinants of protease-substrate recognition. This information is crucial for understanding enzyme function, designing selective inhibitors, and mapping proteolytic pathways in complex biological systems.
Assay Development and Validation: Beyond its use in standard activity assays, the peptide is frequently utilized in the development and validation of novel biochemical assays. Its well-characterized cleavage properties and predictable fluorescence response make it an ideal candidate for optimizing assay conditions, validating new instrumentation, and benchmarking assay performance. By integrating this substrate into assay development pipelines, researchers can ensure the reliability and sensitivity of their experimental systems, supporting a wide range of applications in enzymology, chemical biology, and molecular diagnostics.
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